[unreadable] In eukaryotic cells, proteins destined for the cell surface or for the external milieu are first translocated into the endoplasmic reticulum (ER) where initial protein folding and modifications occur that are essential for the protein to attain its appropriate functional conformation prior to transit to the cell surface. Mutation in the primary amino acid sequence cause protein misfolding and contribute to disease pathogenesis. Recently there have been significant breakthroughs in our fundamental understanding of the cellular machinery that direct protein folding, modification, transport, aggregation, and degradation to ensure fidelity of the final product. In particular new insights show that regulation of disulfide bond formation and carbohydrate modification direct the ultimate destination for the protein. A number of protein chaperones have been identified that interact transiently with folding intermediates and their roles in facilitating protein folding are rapidly being elucidated. It is now evident that cellular responses to protein misfolding contribute to the pathology of numerous disease states and these pathways are rapidly being elucidated. This conference will focus on a novel genetic, biochemical, and cell biological approaches to unravel the complexities of protein folding, processing, and transport within the early secretory pathway in vivo. Identifying the rate limiting steps in secretion will improve the ability to produce complex proteins at high levels from eukaryotic cells. A workshop will be devoted to elucidate the role of protein chaperones in protein folding. Understanding the fundamental processes of how wild-type and mutant proteins fold can be exploited to develop therapeutically useful inhibitors or potentiators for these processes to target pathologies ranging from cancer, infection and immunological disorders, and genetic disease. This conference will focus on new technologies and methodologies to study this rapidly moving field in order to dissect the complexity and diversity of ER function. [unreadable] [unreadable]